Structural Basis for Double-Stranded RNA Processing by Dicer
Howard Hughes Medical Institute · Lawrence Berkeley National Laboratory · +1 more institution
Abstract
The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.
Citation impact
- FWCI
- 23.44
- Percentile
- 100%
- References
- 36
Authors
8- IJIan J. MacRae
Howard Hughes Medical Institute, Lawrence Berkeley National Laboratory, University of California, Berkeley
- KZKaihong Zhou
Howard Hughes Medical Institute, Lawrence Berkeley National Laboratory, University of California, Berkeley
- FLFei Li
Howard Hughes Medical Institute, Lawrence Berkeley National Laboratory, University of California, Berkeley
- ARAdrian Repic
Howard Hughes Medical Institute, Lawrence Berkeley National Laboratory, University of California, Berkeley
- ANAngela N. Brooks
Howard Hughes Medical Institute, Lawrence Berkeley National Laboratory, University of California, Berkeley
Topics & keywords
- Dicer
- Ribonuclease III
- RNA silencing
- RNA
- Ribonuclease
- RNase P
- Nucleotide
- Ribonuclease T1